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Database: PDB
Entry: 4OG5
LinkDB: 4OG5
Original site: 4OG5 
HEADER    PROTEIN BINDING/INHIBITOR               15-JAN-14   4OG5              
TITLE     HUMAN MENIN WITH BOUND INHIBITOR MIV-5                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MENIN;                                                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: MEN1, SCG2;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PROTEIN BINDING-INHIBITOR COMPLEX                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.HE,T.J.SENTER,J.W.POLLOCK,C.HAN,S.K.UPADHYAY,T.PUROHIT,             
AUTHOR   2 R.D.GOGLIOTTI,C.W.LINDSLEY,T.CIERPICKI,S.R.STAUFFER,J.GREMBECKA      
REVDAT   2   19-MAR-14 4OG5    1       JRNL                                     
REVDAT   1   05-MAR-14 4OG5    0                                                
JRNL        AUTH   S.HE,T.J.SENTER,J.POLLOCK,C.HAN,S.K.UPADHYAY,T.PUROHIT,      
JRNL        AUTH 2 R.D.GOGLIOTTI,C.W.LINDSLEY,T.CIERPICKI,S.R.STAUFFER,         
JRNL        AUTH 3 J.GREMBECKA                                                  
JRNL        TITL   HIGH-AFFINITY SMALL-MOLECULE INHIBITORS OF THE MENIN-MIXED   
JRNL        TITL 2 LINEAGE LEUKEMIA (MLL) INTERACTION CLOSELY MIMIC A NATURAL   
JRNL        TITL 3 PROTEIN-PROTEIN INTERACTION.                                 
JRNL        REF    J.MED.CHEM.                   V.  57  1543 2014              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   24472025                                                     
JRNL        DOI    10.1021/JM401868D                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.63 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.63                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.14                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 57894                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.164                           
REMARK   3   R VALUE            (WORKING SET) : 0.163                           
REMARK   3   FREE R VALUE                     : 0.194                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3087                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.63                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.67                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4191                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.13                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2270                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 220                          
REMARK   3   BIN FREE R VALUE                    : 0.2510                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3657                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 76                                      
REMARK   3   SOLVENT ATOMS            : 373                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.08                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.06000                                             
REMARK   3    B22 (A**2) : 0.27000                                              
REMARK   3    B33 (A**2) : -0.21000                                             
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : -0.00000                                             
REMARK   3    B23 (A**2) : -0.00000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.086         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.087         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.060         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.534         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.970                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.958                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3887 ; 0.017 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  3697 ; 0.004 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5274 ; 1.822 ; 1.976       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8475 ; 1.070 ; 3.006       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   482 ; 5.890 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   174 ;30.628 ;23.563       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   629 ;11.521 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    27 ;15.786 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   587 ; 0.115 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4395 ; 0.010 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   916 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1909 ; 2.836 ; 1.995       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1909 ; 2.797 ; 1.997       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2390 ; 3.504 ; 3.111       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  2391 ; 3.515 ; 3.118       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1978 ; 4.383 ; 3.211       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1978 ; 4.379 ; 3.208       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  2882 ; 5.754 ; 4.495       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  4861 ; 8.894 ; 9.500       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  4862 ; 8.893 ; 9.505       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 10                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     2        A    30                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.4860 -10.3640   1.2000              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2844 T22:   0.1629                                     
REMARK   3      T33:   0.3131 T12:   0.0524                                     
REMARK   3      T13:   0.0026 T23:   0.0339                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1169 L22:   2.5787                                     
REMARK   3      L33:   1.5421 L12:   1.1421                                     
REMARK   3      L13:  -0.2935 L23:  -1.0763                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0469 S12:  -0.0916 S13:  -0.2885                       
REMARK   3      S21:  -0.1496 S22:  -0.0083 S23:  -0.1321                       
REMARK   3      S31:   0.3791 S32:   0.2477 S33:   0.0552                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    31        A    97                          
REMARK   3    ORIGIN FOR THE GROUP (A): -12.7830  -3.4030   6.0290              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1500 T22:   0.0533                                     
REMARK   3      T33:   0.1733 T12:  -0.0081                                     
REMARK   3      T13:  -0.0102 T23:   0.0002                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3407 L22:   0.6682                                     
REMARK   3      L33:   1.1239 L12:   0.3742                                     
REMARK   3      L13:   0.0137 L23:  -0.2696                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0596 S12:  -0.1818 S13:  -0.0107                       
REMARK   3      S21:   0.0122 S22:  -0.0512 S23:  -0.0068                       
REMARK   3      S31:   0.1155 S32:  -0.0264 S33:  -0.0083                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    98        A   111                          
REMARK   3    ORIGIN FOR THE GROUP (A): -29.8500 -16.6410 -10.9160              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6091 T22:   0.0657                                     
REMARK   3      T33:   0.4848 T12:  -0.1549                                     
REMARK   3      T13:  -0.1467 T23:   0.0786                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.5219 L22:   8.0163                                     
REMARK   3      L33:   4.5245 L12:   4.0018                                     
REMARK   3      L13:  -3.5999 L23:  -5.9690                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5641 S12:  -0.2103 S13:  -0.7810                       
REMARK   3      S21:  -1.0086 S22:   0.3210 S23:  -0.2199                       
REMARK   3      S31:   0.8311 S32:  -0.1972 S33:   0.2431                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   112        A   202                          
REMARK   3    ORIGIN FOR THE GROUP (A): -24.1970  -0.3710  -8.8600              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1731 T22:   0.0705                                     
REMARK   3      T33:   0.2008 T12:  -0.0295                                     
REMARK   3      T13:  -0.0073 T23:   0.0063                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6168 L22:   0.2355                                     
REMARK   3      L33:   0.5439 L12:  -0.1298                                     
REMARK   3      L13:   0.1706 L23:   0.0717                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0199 S12:  -0.0693 S13:   0.0128                       
REMARK   3      S21:   0.0183 S22:   0.0203 S23:   0.0285                       
REMARK   3      S31:   0.0974 S32:  -0.0881 S33:  -0.0402                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   203        A   235                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.9880   4.5810 -20.7990              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1584 T22:   0.0282                                     
REMARK   3      T33:   0.2047 T12:  -0.0192                                     
REMARK   3      T13:  -0.0066 T23:  -0.0082                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1251 L22:   1.2818                                     
REMARK   3      L33:   1.7441 L12:   0.0310                                     
REMARK   3      L13:   0.1766 L23:  -0.5197                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0273 S12:   0.0506 S13:   0.0993                       
REMARK   3      S21:  -0.1051 S22:  -0.0071 S23:   0.1073                       
REMARK   3      S31:   0.0690 S32:  -0.0742 S33:  -0.0202                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   236        A   336                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.5360  10.9230 -12.0170              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1286 T22:   0.0453                                     
REMARK   3      T33:   0.2097 T12:  -0.0053                                     
REMARK   3      T13:  -0.0047 T23:   0.0061                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3214 L22:   0.3617                                     
REMARK   3      L33:   1.0282 L12:  -0.0294                                     
REMARK   3      L13:   0.2137 L23:  -0.3078                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0198 S12:  -0.0010 S13:   0.0622                       
REMARK   3      S21:   0.0338 S22:  -0.0695 S23:  -0.0748                       
REMARK   3      S31:  -0.0260 S32:   0.1537 S33:   0.0893                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   337        A   428                          
REMARK   3    ORIGIN FOR THE GROUP (A): -10.0330  27.7830 -22.1010              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1635 T22:   0.0714                                     
REMARK   3      T33:   0.2300 T12:  -0.0026                                     
REMARK   3      T13:  -0.0062 T23:   0.0066                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5472 L22:   0.6931                                     
REMARK   3      L33:   0.5954 L12:   0.2262                                     
REMARK   3      L13:  -0.0241 L23:  -0.0690                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0303 S12:  -0.0529 S13:  -0.0039                       
REMARK   3      S21:  -0.0314 S22:  -0.0148 S23:  -0.0080                       
REMARK   3      S31:  -0.0014 S32:   0.0458 S33:   0.0451                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   429        A   460                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.8920  36.6340 -27.4930              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1980 T22:   0.0900                                     
REMARK   3      T33:   0.2408 T12:   0.0120                                     
REMARK   3      T13:  -0.0126 T23:   0.0146                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7716 L22:   1.5761                                     
REMARK   3      L33:   1.5837 L12:   1.7283                                     
REMARK   3      L13:  -1.7724 L23:  -0.6900                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0768 S12:   0.0473 S13:   0.0247                       
REMARK   3      S21:  -0.1009 S22:   0.0610 S23:   0.0384                       
REMARK   3      S31:  -0.1035 S32:  -0.0558 S33:   0.0158                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   461        A   580                          
REMARK   3    ORIGIN FOR THE GROUP (A): -12.9650  36.6730 -33.3790              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1880 T22:   0.0399                                     
REMARK   3      T33:   0.2175 T12:   0.0117                                     
REMARK   3      T13:  -0.0446 T23:   0.0062                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4553 L22:   4.2712                                     
REMARK   3      L33:   0.4037 L12:  -0.5399                                     
REMARK   3      L13:   0.3705 L23:   0.5419                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0740 S12:   0.0820 S13:   0.1693                       
REMARK   3      S21:  -0.0497 S22:   0.0414 S23:  -0.3059                       
REMARK   3      S31:  -0.1173 S32:   0.0458 S33:   0.0326                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   581        A   588                          
REMARK   3    ORIGIN FOR THE GROUP (A): -29.2510  44.6170 -29.4680              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5323 T22:   0.3539                                     
REMARK   3      T33:   0.4230 T12:   0.0433                                     
REMARK   3      T13:  -0.0337 T23:   0.1426                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  30.9854 L22:  54.8602                                     
REMARK   3      L33:   1.5917 L12: -10.0964                                     
REMARK   3      L13:   2.6103 L23:  -9.2520                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3107 S12:  -2.2213 S13:  -0.6187                       
REMARK   3      S21:   1.3353 S22:   0.2183 S23:  -1.0648                       
REMARK   3      S31:  -0.2280 S32:  -0.1317 S33:   0.0923                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4OG5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JAN-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB084450.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-AUG-12                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 8                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-F                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97872                            
REMARK 200  MONOCHROMATOR                  : C(111)                             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 61076                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.630                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.140                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 23.4700                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 4GPQ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.49                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM ACETATE, 0.1 M HEPES PH   
REMARK 280  7.5 AND 25% W/V PEG 3,350. THIS SOLUTION WAS MIXED 1:1 WITH         
REMARK 280  2.5MG/ML PROTEIN IN 50MM TRIS-HCL (PH 8.0), 50MM NACL, AND 1MM      
REMARK 280  TCEP. PRIOR TO DATA COLLECTION, CRYSTALS WERE TRANSFERRED INTO A    
REMARK 280  CRYO-SOLUTION CONTAINING 20% PEG550 MME AND FLASH-FROZEN IN         
REMARK 280  LIQUID NITROGEN, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 283K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       24.33150            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       62.23200            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       40.06550            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       62.23200            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.33150            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       40.06550            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -4                                                      
REMARK 465     GLY A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     LYS A   589                                                      
REMARK 465     GLN A   590                                                      
REMARK 465     LYS A   591                                                      
REMARK 465     VAL A   592                                                      
REMARK 465     SER A   593                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A 109    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 131    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A 136    CG   OD1  OD2                                       
REMARK 470     LYS A 201    CG   CD   CE   NZ                                   
REMARK 470     GLU A 204    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 249    CG   CD1  CD2                                       
REMARK 470     ARG A 355    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 358    CG   CD   OE1  OE2                                  
REMARK 470     VAL A 460    CG1  CG2                                            
REMARK 470     PRO A 461    O                                                   
REMARK 470     ALA A 548    N    CB                                             
REMARK 470     LYS A 569    CG   CD   CE   NZ                                   
REMARK 470     GLN A 586    CG   CD   OE1  NE2                                  
REMARK 470     MET A 587    CG   SD   CE                                        
REMARK 470     LYS A 588    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TYR A  77      -62.87   -158.44                                   
REMARK 500    ASP A 180       10.81   -147.36                                   
REMARK 500    ASN A 189       19.10     55.20                                   
REMARK 500    SER A 226       42.63    -87.44                                   
REMARK 500    GLU A 356       -4.86     84.05                                   
REMARK 500    ASP A 370      -55.14   -141.93                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     TBF A  609                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2S7 A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TBF A 609                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4OG3   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4OG4   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4OG6   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4OG7   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4OG8   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE CRYSTALLIZED SEQUENCE CORRESPONDS TO THE HUMAN MENIN ISOFORM 2   
DBREF  4OG5 A    1   593  UNP    O00255   MEN1_HUMAN       1    593             
SEQADV 4OG5 GLY A   -4  UNP  O00255              EXPRESSION TAG                 
SEQADV 4OG5 GLY A   -3  UNP  O00255              EXPRESSION TAG                 
SEQADV 4OG5 SER A   -2  UNP  O00255              EXPRESSION TAG                 
SEQADV 4OG5 SER A   -1  UNP  O00255              EXPRESSION TAG                 
SEQADV 4OG5 SER A    0  UNP  O00255              EXPRESSION TAG                 
SEQADV 4OG5     A       UNP  O00255    ILE    54 DELETION                       
SEQADV 4OG5     A       UNP  O00255    PRO    55 DELETION                       
SEQADV 4OG5     A       UNP  O00255    THR    56 DELETION                       
SEQADV 4OG5     A       UNP  O00255    ASN    57 DELETION                       
SEQADV 4OG5     A       UNP  O00255    VAL    58 DELETION                       
SEQADV 4OG5     A       UNP  O00255    PRO    59 DELETION                       
SEQADV 4OG5     A       UNP  O00255    GLU    60 DELETION                       
SEQADV 4OG5     A       UNP  O00255    LEU    61 DELETION                       
SEQADV 4OG5     A       UNP  O00255    THR    62 DELETION                       
SEQADV 4OG5     A       UNP  O00255    PHE    63 DELETION                       
SEQADV 4OG5     A       UNP  O00255    GLN    64 DELETION                       
SEQADV 4OG5     A       UNP  O00255    PRO    65 DELETION                       
SEQADV 4OG5     A       UNP  O00255    SER    66 DELETION                       
SEQADV 4OG5     A       UNP  O00255    PRO    67 DELETION                       
SEQADV 4OG5     A       UNP  O00255    ALA    68 DELETION                       
SEQADV 4OG5     A       UNP  O00255    PRO    69 DELETION                       
SEQADV 4OG5     A       UNP  O00255    ASP    70 DELETION                       
SEQADV 4OG5     A       UNP  O00255    PRO    71 DELETION                       
SEQADV 4OG5     A       UNP  O00255    PRO    72 DELETION                       
SEQADV 4OG5     A       UNP  O00255    GLY    73 DELETION                       
SEQADV 4OG5     A       UNP  O00255    GLU   387 DELETION                       
SEQADV 4OG5     A       UNP  O00255    GLU   388 DELETION                       
SEQADV 4OG5     A       UNP  O00255    ARG   389 DELETION                       
SEQADV 4OG5     A       UNP  O00255    PRO   390 DELETION                       
SEQADV 4OG5     A       UNP  O00255    GLY   391 DELETION                       
SEQADV 4OG5     A       UNP  O00255    GLU   392 DELETION                       
SEQADV 4OG5     A       UNP  O00255    GLN   393 DELETION                       
SEQADV 4OG5     A       UNP  O00255    SER   394 DELETION                       
SEQADV 4OG5     A       UNP  O00255    GLN   395 DELETION                       
SEQADV 4OG5     A       UNP  O00255    GLY   396 DELETION                       
SEQADV 4OG5     A       UNP  O00255    THR   397 DELETION                       
SEQADV 4OG5     A       UNP  O00255    GLN   398 DELETION                       
SEQADV 4OG5     A       UNP  O00255    ARG   460 DELETION                       
SEQADV 4OG5     A       UNP  O00255    GLU   461 DELETION                       
SEQADV 4OG5     A       UNP  O00255    ALA   462 DELETION                       
SEQADV 4OG5     A       UNP  O00255    GLU   463 DELETION                       
SEQADV 4OG5     A       UNP  O00255    ALA   464 DELETION                       
SEQADV 4OG5     A       UNP  O00255    ALA   465 DELETION                       
SEQADV 4OG5     A       UNP  O00255    GLU   466 DELETION                       
SEQADV 4OG5     A       UNP  O00255    ALA   467 DELETION                       
SEQADV 4OG5     A       UNP  O00255    GLU   468 DELETION                       
SEQADV 4OG5     A       UNP  O00255    GLU   469 DELETION                       
SEQADV 4OG5     A       UNP  O00255    PRO   470 DELETION                       
SEQADV 4OG5     A       UNP  O00255    TRP   471 DELETION                       
SEQADV 4OG5     A       UNP  O00255    GLY   472 DELETION                       
SEQADV 4OG5     A       UNP  O00255    GLU   473 DELETION                       
SEQADV 4OG5     A       UNP  O00255    GLU   474 DELETION                       
SEQADV 4OG5     A       UNP  O00255    ALA   475 DELETION                       
SEQADV 4OG5     A       UNP  O00255    ARG   476 DELETION                       
SEQADV 4OG5     A       UNP  O00255    GLU   477 DELETION                       
SEQADV 4OG5     A       UNP  O00255    GLY   478 DELETION                       
SEQADV 4OG5     A       UNP  O00255    ARG   479 DELETION                       
SEQADV 4OG5     A       UNP  O00255    ARG   480 DELETION                       
SEQADV 4OG5     A       UNP  O00255    ARG   481 DELETION                       
SEQADV 4OG5     A       UNP  O00255    GLY   482 DELETION                       
SEQADV 4OG5     A       UNP  O00255    PRO   483 DELETION                       
SEQADV 4OG5     A       UNP  O00255    ARG   484 DELETION                       
SEQADV 4OG5     A       UNP  O00255    ARG   485 DELETION                       
SEQADV 4OG5     A       UNP  O00255    GLU   486 DELETION                       
SEQADV 4OG5     A       UNP  O00255    SER   487 DELETION                       
SEQADV 4OG5     A       UNP  O00255    LYS   488 DELETION                       
SEQADV 4OG5     A       UNP  O00255    PRO   489 DELETION                       
SEQADV 4OG5     A       UNP  O00255    GLU   490 DELETION                       
SEQADV 4OG5     A       UNP  O00255    GLU   491 DELETION                       
SEQADV 4OG5     A       UNP  O00255    PRO   492 DELETION                       
SEQADV 4OG5     A       UNP  O00255    PRO   493 DELETION                       
SEQADV 4OG5     A       UNP  O00255    PRO   494 DELETION                       
SEQADV 4OG5     A       UNP  O00255    PRO   495 DELETION                       
SEQADV 4OG5     A       UNP  O00255    LYS   496 DELETION                       
SEQADV 4OG5     A       UNP  O00255    LYS   497 DELETION                       
SEQADV 4OG5     A       UNP  O00255    PRO   498 DELETION                       
SEQADV 4OG5     A       UNP  O00255    ALA   499 DELETION                       
SEQADV 4OG5     A       UNP  O00255    LEU   500 DELETION                       
SEQADV 4OG5     A       UNP  O00255    ASP   501 DELETION                       
SEQADV 4OG5     A       UNP  O00255    LYS   502 DELETION                       
SEQADV 4OG5     A       UNP  O00255    GLY   503 DELETION                       
SEQADV 4OG5     A       UNP  O00255    LEU   504 DELETION                       
SEQADV 4OG5     A       UNP  O00255    GLY   505 DELETION                       
SEQADV 4OG5     A       UNP  O00255    THR   506 DELETION                       
SEQADV 4OG5     A       UNP  O00255    GLY   507 DELETION                       
SEQADV 4OG5     A       UNP  O00255    GLN   508 DELETION                       
SEQADV 4OG5     A       UNP  O00255    GLY   509 DELETION                       
SEQADV 4OG5     A       UNP  O00255    ALA   510 DELETION                       
SEQADV 4OG5     A       UNP  O00255    VAL   511 DELETION                       
SEQADV 4OG5     A       UNP  O00255    SER   512 DELETION                       
SEQADV 4OG5     A       UNP  O00255    GLY   513 DELETION                       
SEQADV 4OG5     A       UNP  O00255    PRO   514 DELETION                       
SEQADV 4OG5     A       UNP  O00255    PRO   515 DELETION                       
SEQADV 4OG5     A       UNP  O00255    ARG   516 DELETION                       
SEQADV 4OG5     A       UNP  O00255    LYS   517 DELETION                       
SEQADV 4OG5     A       UNP  O00255    PRO   518 DELETION                       
SEQADV 4OG5     A       UNP  O00255    PRO   519 DELETION                       
SEQADV 4OG5     A       UNP  O00255    GLY   520 DELETION                       
SEQADV 4OG5     A       UNP  O00255    THR   521 DELETION                       
SEQADV 4OG5     A       UNP  O00255    VAL   522 DELETION                       
SEQADV 4OG5     A       UNP  O00255    ALA   523 DELETION                       
SEQADV 4OG5     A       UNP  O00255    GLY   524 DELETION                       
SEQADV 4OG5     A       UNP  O00255    THR   525 DELETION                       
SEQADV 4OG5     A       UNP  O00255    ALA   526 DELETION                       
SEQADV 4OG5     A       UNP  O00255    ARG   527 DELETION                       
SEQADV 4OG5     A       UNP  O00255    GLY   528 DELETION                       
SEQADV 4OG5     A       UNP  O00255    PRO   529 DELETION                       
SEQADV 4OG5     A       UNP  O00255    GLU   530 DELETION                       
SEQADV 4OG5     A       UNP  O00255    GLY   531 DELETION                       
SEQADV 4OG5     A       UNP  O00255    GLY   532 DELETION                       
SEQADV 4OG5     A       UNP  O00255    SER   533 DELETION                       
SEQADV 4OG5     A       UNP  O00255    THR   534 DELETION                       
SEQADV 4OG5     A       UNP  O00255    ALA   535 DELETION                       
SEQADV 4OG5     A       UNP  O00255    GLN   536 DELETION                       
SEQADV 4OG5     A       UNP  O00255    PRO   540 DELETION                       
SEQADV 4OG5     A       UNP  O00255    THR   541 DELETION                       
SEQADV 4OG5     A       UNP  O00255    ALA   542 DELETION                       
SEQADV 4OG5     A       UNP  O00255    SER   543 DELETION                       
SEQADV 4OG5     A       UNP  O00255    PRO   544 DELETION                       
SEQADV 4OG5     A       UNP  O00255    PRO   545 DELETION                       
SEQADV 4OG5     A       UNP  O00255    PRO   546 DELETION                       
SEQADV 4OG5     A       UNP  O00255    GLU   547 DELETION                       
SEQADV 4OG5     A       UNP  O00255    GLY   548 DELETION                       
SEQRES   1 A  480  GLY GLY SER SER SER MET GLY LEU LYS ALA ALA GLN LYS          
SEQRES   2 A  480  THR LEU PHE PRO LEU ARG SER ILE ASP ASP VAL VAL ARG          
SEQRES   3 A  480  LEU PHE ALA ALA GLU LEU GLY ARG GLU GLU PRO ASP LEU          
SEQRES   4 A  480  VAL LEU LEU SER LEU VAL LEU GLY PHE VAL GLU HIS PHE          
SEQRES   5 A  480  LEU ALA VAL ASN ARG VAL GLY LEU THR TYR PHE PRO VAL          
SEQRES   6 A  480  ALA ASP LEU SER ILE ILE ALA ALA LEU TYR ALA ARG PHE          
SEQRES   7 A  480  THR ALA GLN ILE ARG GLY ALA VAL ASP LEU SER LEU TYR          
SEQRES   8 A  480  PRO ARG GLU GLY GLY VAL SER SER ARG GLU LEU VAL LYS          
SEQRES   9 A  480  LYS VAL SER ASP VAL ILE TRP ASN SER LEU SER ARG SER          
SEQRES  10 A  480  TYR PHE LYS ASP ARG ALA HIS ILE GLN SER LEU PHE SER          
SEQRES  11 A  480  PHE ILE THR GLY THR LYS LEU ASP SER SER GLY VAL ALA          
SEQRES  12 A  480  PHE ALA VAL VAL GLY ALA CYS GLN ALA LEU GLY LEU ARG          
SEQRES  13 A  480  ASP VAL HIS LEU ALA LEU SER GLU ASP HIS ALA TRP VAL          
SEQRES  14 A  480  VAL PHE GLY PRO ASN GLY GLU GLN THR ALA GLU VAL THR          
SEQRES  15 A  480  TRP HIS GLY LYS GLY ASN GLU ASP ARG ARG GLY GLN THR          
SEQRES  16 A  480  VAL ASN ALA GLY VAL ALA GLU ARG SER TRP LEU TYR LEU          
SEQRES  17 A  480  LYS GLY SER TYR MET ARG CYS ASP ARG LYS MET GLU VAL          
SEQRES  18 A  480  ALA PHE MET VAL CYS ALA ILE ASN PRO SER ILE ASP LEU          
SEQRES  19 A  480  HIS THR ASP SER LEU GLU LEU LEU GLN LEU GLN GLN LYS          
SEQRES  20 A  480  LEU LEU TRP LEU LEU TYR ASP LEU GLY HIS LEU GLU ARG          
SEQRES  21 A  480  TYR PRO MET ALA LEU GLY ASN LEU ALA ASP LEU GLU GLU          
SEQRES  22 A  480  LEU GLU PRO THR PRO GLY ARG PRO ASP PRO LEU THR LEU          
SEQRES  23 A  480  TYR HIS LYS GLY ILE ALA SER ALA LYS THR TYR TYR ARG          
SEQRES  24 A  480  ASP GLU HIS ILE TYR PRO TYR MET TYR LEU ALA GLY TYR          
SEQRES  25 A  480  HIS CYS ARG ASN ARG ASN VAL ARG GLU ALA LEU GLN ALA          
SEQRES  26 A  480  TRP ALA ASP THR ALA THR VAL ILE GLN ASP TYR ASN TYR          
SEQRES  27 A  480  CYS ARG GLU ASP GLU GLU ILE TYR LYS GLU PHE PHE GLU          
SEQRES  28 A  480  VAL ALA ASN ASP VAL ILE PRO ASN LEU LEU LYS GLU ALA          
SEQRES  29 A  480  ALA SER LEU LEU GLU ALA GLY SER GLN GLY SER ALA LEU          
SEQRES  30 A  480  GLN ASP PRO GLU CYS PHE ALA HIS LEU LEU ARG PHE TYR          
SEQRES  31 A  480  ASP GLY ILE CYS LYS TRP GLU GLU GLY SER PRO THR PRO          
SEQRES  32 A  480  VAL LEU HIS VAL GLY TRP ALA THR PHE LEU VAL GLN SER          
SEQRES  33 A  480  LEU GLY ARG PHE GLU GLY GLN VAL ARG GLN LYS VAL ARG          
SEQRES  34 A  480  ILE VAL SER VAL PRO ALA PRO VAL LEU THR PHE GLN SER          
SEQRES  35 A  480  GLU LYS MET LYS GLY MET LYS GLU LEU LEU VAL ALA THR          
SEQRES  36 A  480  LYS ILE ASN SER SER ALA ILE LYS LEU GLN LEU THR ALA          
SEQRES  37 A  480  GLN SER GLN VAL GLN MET LYS LYS GLN LYS VAL SER              
HET    2S7  A 601      31                                                       
HET    SO4  A 602       5                                                       
HET    SO4  A 603       5                                                       
HET    PG4  A 604      13                                                       
HET    PEG  A 605       7                                                       
HET    DMS  A 606       4                                                       
HET    DMS  A 607       4                                                       
HET    DMS  A 608       4                                                       
HET    TBF  A 609       3                                                       
HETNAM     2S7 4-(3-{4-[(S)-CYCLOPENTYL(HYDROXY)PYRIDIN-2-                      
HETNAM   2 2S7  YLMETHYL]PIPERIDIN-1-YL}PROPOXY)BENZONITRILE                    
HETNAM     SO4 SULFATE ION                                                      
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     DMS DIMETHYL SULFOXIDE                                               
HETNAM     TBF TERT-BUTYL FORMATE                                               
HETSYN     TBF TERTIARY BUTOXY CARBONYL                                         
FORMUL   2  2S7    C26 H33 N3 O2                                                
FORMUL   3  SO4    2(O4 S 2-)                                                   
FORMUL   5  PG4    C8 H18 O5                                                    
FORMUL   6  PEG    C4 H10 O3                                                    
FORMUL   7  DMS    3(C2 H6 O S)                                                 
FORMUL  10  TBF    C5 H10 O2                                                    
FORMUL  11  HOH   *373(H2 O)                                                    
HELIX    1   1 LYS A    4  THR A    9  1                                   6    
HELIX    2   2 SER A   15  GLY A   28  1                                  14    
HELIX    3   3 ASP A   33  VAL A   50  1                                  18    
HELIX    4   4 ASP A   82  VAL A  101  1                                  20    
HELIX    5   5 ASP A  102  TYR A  106  5                                   5    
HELIX    6   6 ARG A  108  VAL A  112  5                                   5    
HELIX    7   7 SER A  114  SER A  128  1                                  15    
HELIX    8   8 SER A  142  THR A  150  1                                   9    
HELIX    9   9 ASP A  153  LEU A  168  1                                  16    
HELIX   10  10 GLY A  187  GLU A  191  5                                   5    
HELIX   11  11 VAL A  211  GLU A  217  1                                   7    
HELIX   12  12 SER A  219  SER A  226  5                                   8    
HELIX   13  13 ASP A  231  ALA A  242  1                                  12    
HELIX   14  14 SER A  253  LEU A  270  1                                  18    
HELIX   15  15 TYR A  276  GLU A  290  1                                  15    
HELIX   16  16 ASP A  297  TYR A  313  1                                  17    
HELIX   17  17 ILE A  318  ASN A  331  1                                  14    
HELIX   18  18 ASN A  333  GLN A  349  1                                  17    
HELIX   19  19 ASP A  357  ASP A  370  1                                  14    
HELIX   20  20 ASP A  370  ALA A  385  1                                  16    
HELIX   21  21 SER A  402  GLN A  405  5                                   4    
HELIX   22  22 ASP A  406  GLU A  425  1                                  20    
HELIX   23  23 HIS A  433  ARG A  446  1                                  14    
HELIX   24  24 GLU A  448  GLN A  453  1                                   6    
HELIX   25  25 SER A  555  LYS A  562  1                                   8    
HELIX   26  26 GLU A  563  VAL A  566  5                                   4    
HELIX   27  27 ASN A  571  ALA A  581  1                                  11    
SHEET    1   A 4 GLN A 192  ALA A 194  0                                        
SHEET    2   A 4 ALA A 182  PHE A 186 -1  N  VAL A 184   O  ALA A 194           
SHEET    3   A 4 HIS A 174  LEU A 177 -1  N  ALA A 176   O  TRP A 183           
SHEET    4   A 4 MET A 228  ARG A 229 -1  O  MET A 228   N  LEU A 177           
SHEET    1   B 2 SER A 246  ASP A 248  0                                        
SHEET    2   B 2 THR A 251  ASP A 252 -1  O  THR A 251   N  ILE A 247           
SHEET    1   C 2 ARG A 456  VAL A 458  0                                        
SHEET    2   C 2 VAL A 550  THR A 552  1  O  LEU A 551   N  ARG A 456           
CISPEP   1 PHE A   11    PRO A   12          0         4.18                     
SITE     1 AC1 17 SER A 155  SER A 178  GLU A 179  HIS A 181                    
SITE     2 AC1 17 PHE A 238  ALA A 242  TYR A 276  MET A 278                    
SITE     3 AC1 17 TYR A 319  MET A 322  TYR A 323  TRP A 341                    
SITE     4 AC1 17 GLU A 363  TBF A 609  HOH A 943  HOH A 970                    
SITE     5 AC1 17 HOH A 982                                                     
SITE     1 AC2  5 TYR A 133  PHE A 134  ARG A 137  LYS A 151                    
SITE     2 AC2  5 ARG A 332                                                     
SITE     1 AC3  2 ARG A  14  HOH A 827                                          
SITE     1 AC4  5 LEU A  75  THR A  76  PHE A 365  HOH A 730                    
SITE     2 AC4  5 HOH A 937                                                     
SITE     1 AC5  3 TRP A 126  LYS A 135  TRP A 198                               
SITE     1 AC6  5 PHE A  43  PHE A  47  GLY A 386  HOH A 868                    
SITE     2 AC6  5 HOH A 986                                                     
SITE     1 AC7  5 ARG A 332  VAL A 334  ARG A 335  ALA A 403                    
SITE     2 AC7  5 HOH A 820                                                     
SITE     1 AC8  6 VAL A 185  GLY A 190  GLU A 191  TYR A 227                    
SITE     2 AC8  6 ARG A 229  SER A 583                                          
SITE     1 AC9  3 2S7 A 601  HOH A 887  HOH A 970                               
CRYST1   48.663   80.131  124.464  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.020549  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012480  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008034        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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